Repetitive architecture of the Haemophilus influenzae Hia trimeric autotransporter.
The Hia autotransporter of Haemophilus influenzae belongs to the trimeric autotransporter subfamily and mediates bacterial adherence to the respiratory epithelium. In this report, we show that the structure of Hia is characterized by a modular architecture containing repeats of structurally distinct domains. Comparison of the structures of HiaBD1 and HiaBD2 adhesive repeats and a nonadhesive repeat (a novel fold) shed light on the structural determinants of Hia adhesive function. Examination of the structure of an extended version of the Hia translocator domain revealed the structural transition between the C-terminal translocator domain and the N-terminal passenger domain, highlighting a highly intertwined domain that is ubiquitous among trimeric autotransporters. Overall, this study provides important insights into the mechanism of Hia adhesive activity and the overall structure of trimeric autotransporters.
Meng
Guoyu
G
Institute of Structural and Molecular Biology at UCL/Birkbeck, London, UK.
St Geme
Joseph W
JW
Waksman
Gabriel
G
D018829:Adhesins, Bacterial / Q000737:chemistry*; D000595:Amino Acid Sequence; D001422:Bacterial Adhesion; D002352:Carrier Proteins / Q000737:chemistry*; D018360:Crystallography, X-Ray; D006193:Haemophilus influenzae / Q000737:chemistry* / Q000502:physiology*; D008954:Models, Biological; D008958:Models, Molecular; D008969:Molecular Sequence Data; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment
D018829:Adhesins, Bacterial; D002352:Carrier Proteins